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Q9P996

- PSB_ARCFU

UniProt

Q9P996 - PSB_ARCFU

Protein

Proteasome subunit beta

Gene

psmB

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.UniRule annotation

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.UniRule annotation

    Enzyme regulationi

    The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei12 – 121NucleophileUniRule annotation

    GO - Molecular functioni

    1. threonine-type endopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. proteasomal protein catabolic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciAFUL224325:GJBC-494-MONOMER.

    Protein family/group databases

    MEROPSiT01.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit betaUniRule annotation (EC:3.4.25.1UniRule annotation)
    Alternative name(s):
    20S proteasome beta subunitUniRule annotation
    Proteasome core protein PsmBUniRule annotation
    Gene namesi
    Name:psmBUniRule annotation
    Ordered Locus Names:AF_0481
    OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
    Taxonomic identifieri224325 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
    ProteomesiUP000002199: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. proteasome core complex, beta-subunit complex Source: UniProtKB-HAMAP

    Keywords - Cellular componenti

    Cytoplasm, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 1111Removed in mature form; by autocatalysisUniRule annotationPRO_0000026659Add
    BLAST
    Chaini12 – 213202Proteasome subunit betaPRO_0000026660Add
    BLAST

    Keywords - PTMi

    Autocatalytic cleavage, Zymogen

    Interactioni

    Subunit structurei

    The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has probably a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is likely capped at one or both ends by the proteasome regulatory ATPase, PAN.1 Publication

    Protein-protein interaction databases

    IntActiQ9P996. 1 interaction.
    STRINGi224325.AF0481.

    Structurei

    Secondary structure

    1
    213
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 196
    Beta strandi22 – 287
    Beta strandi31 – 333
    Beta strandi36 – 416
    Beta strandi45 – 495
    Beta strandi52 – 587
    Helixi60 – 8122
    Helixi87 – 10014
    Turni101 – 1033
    Beta strandi108 – 1169
    Beta strandi119 – 1257
    Beta strandi131 – 14111
    Helixi144 – 15411
    Helixi161 – 17616
    Beta strandi186 – 1916
    Beta strandi196 – 1983
    Helixi200 – 2078
    Helixi208 – 2103

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J2QX-ray2.83H/I/J/K/L/M/N12-213[»]
    ProteinModelPortaliQ9P996.
    SMRiQ9P996. Positions 12-213.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P996.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    KOiK03433.
    OMAiMVDWLGT.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    HAMAPiMF_02113_A. Proteasome_B_A.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR019983. Pept_T1A_Psome_bsu_arc.
    IPR000243. Pept_T1A_subB.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    PRINTSiPR00141. PROTEASOME.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR03634. arc_protsome_B. 1 hit.
    PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9P996-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSMIEEKIYK GTTTVGLVCK DGVVMATEKR ATMGNFIASK AAKKIYQIAD    50
    RMAMTTAGSV GDAQFLARII KIEANLYEIR RERKPTVRAI ATLTSNLLNS 100
    YRYFPYLVQL LIGGIDSEGK SIYSIDPIGG AIEEKDIVAT GSGSLTAYGV 150
    LEDRFTPEIG VDEAVELAVR AIYSAMKRDS ASGDGIDVVK ITEDEFYQYS 200
    PEEVEQILAK FRK 213
    Length:213
    Mass (Da):23,418
    Last modified:October 1, 2000 - v1
    Checksum:iDA03E480A88F8227
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB90757.1.
    PIRiA69310.
    RefSeqiNP_069317.1. NC_000917.1.

    Genome annotation databases

    EnsemblBacteriaiAAB90757; AAB90757; AF_0481.
    GeneIDi1483698.
    KEGGiafu:AF0481.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB90757.1 .
    PIRi A69310.
    RefSeqi NP_069317.1. NC_000917.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J2Q X-ray 2.83 H/I/J/K/L/M/N 12-213 [» ]
    ProteinModelPortali Q9P996.
    SMRi Q9P996. Positions 12-213.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9P996. 1 interaction.
    STRINGi 224325.AF0481.

    Protein family/group databases

    MEROPSi T01.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB90757 ; AAB90757 ; AF_0481 .
    GeneIDi 1483698.
    KEGGi afu:AF0481.

    Phylogenomic databases

    eggNOGi COG0638.
    KOi K03433.
    OMAi MVDWLGT.

    Enzyme and pathway databases

    BioCyci AFUL224325:GJBC-494-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9P996.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    HAMAPi MF_02113_A. Proteasome_B_A.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR019983. Pept_T1A_Psome_bsu_arc.
    IPR000243. Pept_T1A_subB.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PRINTSi PR00141. PROTEASOME.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    TIGRFAMsi TIGR03634. arc_protsome_B. 1 hit.
    PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
      Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
      , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
      Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
    2. "Investigations on the maturation and regulation of archaebacterial proteasomes."
      Groll M., Brandstetter H., Bartunik H., Bourenkow G., Huber R.
      J. Mol. Biol. 327:75-83(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 12-213 IN COMPLEX WITH ALPHA SUBUNIT AND CALPAIN-INHIBITOR I, SUBUNIT.

    Entry informationi

    Entry nameiPSB_ARCFU
    AccessioniPrimary (citable) accession number: Q9P996
    Secondary accession number(s): O29769
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3